Index to Course Material
Index to Section 10
Alpha/Beta Folds
Alpha+Beta Folds
The doubly wound alpha/beta topology was described on the
previous page. Some variations of the classic
doubly wound fold are illustrated here. In the topology diagrams below, the
parts of the chain linking the beta-strands are red, and are thick when they
include an alpha-helix. In the RasMol scripts, non-alpha-helical linking regions
are shown in pink. Some of the scripts highlight in blue where the fold begins.
flavodoxin, 1flv (127Kb) [Bbk|BNL|ExP|Waw|Hal] ... SCRIPT
subtilisin, 1sbt (172Kb) [Bbk|BNL|ExP|Waw|Hal] ... SCRIPT
arabinose-binding protein, domain 1, 5abp (217Kb) [Bbk|BNL|ExP|Waw|Hal] ... SCRIPT
glyceraldehyde phosphate dehydrogenase, 3gpd (443Kb) [Bbk|BNL|ExP|Waw|Hal] ... SCRIPT
dihydrofolate reductase, 3dfr (157Kb) [Bbk|BNL|ExP|Waw|Hal]
adenylate kinase, 3adk (135Kb) [Bbk|BNL|ExP|Waw|Hal]
rhodanese domain 1, 1rhd (202Kb) [Bbk|BNL|ExP|Waw|Hal]
glutathione reductase, 1gra (366Kb) [Bbk|BNL|ExP|Waw|Hal]
carboxypeptidase, 2ctb (Kb) [Bbk|BNL|ExP|Waw|Hal] This fold varies considerably from a classic doubly-wound variation in order to achieve the arrangement of sheet (mixed parallel and antiparallel in this case).
Last updated 17th Jun '96